By Robert P. Mecham

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This allowed t h e pore size in elastin to be calculated from t h e data for each solute. The v a l u e s of t h e effective pore diameter calculated for sugars and glycols r a n g i n g in molecular w e i g h t from 60 to 1,000 were almost constant, at 3 0 - 3 3 A. I took t h e precaution of sending t h e draft paper to Prof. T. C. Laurent in U p p s a l a before publication and almost i m m e e Ό REFLECTIONS ON A CAREER 23 diately received a reply t h a t h e h a d plotted t h e chromatographic data according to t h e equation of Siegel and Monty (52) and t h a t t h e points fell on a rather good straight line, indicating t h a t t h e data were also valid for a gel consisting of a s y s t e m of parallel hydrated molecular rods of 8 A radius (46).

F. (1950). Nature (London) 1 6 5 , 62. Sanger, F. (1945). Biochem. J. 3 9 , 567. Adair, G. , Davis, H. , and Partridge, S. M. (1951). Nature (London) 1 6 7 , 605. Partridge, S. M. (1962). Adv. Protein Chem. 1 7 (Review). , Stern, P. , Elsden, D. , and Partridge, S. M. (1963). Biochem. J. 8 7 , 3 4 4 . Hoeve, S. A. , and Flory, P. J. (1958). J. Am. Chem. Soc. 8 0 , 6523. Partridge, S. , Davis, H. , and Adair, G. S. (1955). Biochem. J. 6 1 , 11. Partridge, S. , and Davis, H. F. (1955). Biochem. J.

Modifications In t h e l u m e n of t h e RER, n e w l y synthesized procollagen undergoes hydroxylation of specific proline and lysine residues by t h e actions of prolyl-4-hydroxylase, prolyl-3-hydroxylase, and lysyl hydroxylase (Kivirikko and Myllyla, 1981). A l t h o u g h three separate e n z y m e s me­ diate t h e s e activities, all three share t h e requirement for t h e presence of molecular oxygen, F e , ascorbate, and α-ketoglutarate as cofactors (Kivirikko and Myllyla, 1981). The hydroxylation of specific residues is sequence specific (Bornstein and Traub, 1979).

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